GNE_PLESH
ID GNE_PLESH Reviewed; 345 AA.
AC Q7BJX9;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=UDP-N-acetylglucosamine 4-epimerase;
DE EC=5.1.3.7 {ECO:0000269|PubMed:12484781, ECO:0000269|PubMed:21810411};
DE AltName: Full=UDP-GalNAc 4-epimerase {ECO:0000303|PubMed:21384454, ECO:0000303|PubMed:21810411};
GN Name=wbgU {ECO:0000312|EMBL:AAG17409.1};
OS Plesiomonas shigelloides (Aeromonas shigelloides).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Plesiomonas.
OX NCBI_TaxID=703 {ECO:0000312|EMBL:AAG17409.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=C27 {ECO:0000312|EMBL:AAG17409.1};
RX PubMed=10992522; DOI=10.1128/iai.68.10.6056-6061.2000;
RA Shepherd J.G., Wang L., Reeves P.R.;
RT "Comparison of O-antigen gene clusters of Escherichia coli (Shigella)
RT sonnei and Plesiomonas shigelloides O17: sonnei gained its current plasmid-
RT borne O-antigen genes from P. shigelloides in a recent event.";
RL Infect. Immun. 68:6056-6061(2000).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES,
RP SUBUNIT, AND PATHWAY.
RX PubMed=12484781; DOI=10.1021/bi026384i;
RA Kowal P., Wang P.G.;
RT "New UDP-GlcNAc C4 epimerase involved in the biosynthesis of 2-acetamino-2-
RT deoxy-L-altruronic acid in the O-antigen repeating units of Plesiomonas
RT shigelloides O17.";
RL Biochemistry 41:15410-15414(2002).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF MUTANT ALA-305 IN COMPLEX WITH
RP NAD AND UDP-N-ACETYL-ALPHA-D-GALACTOSAMINE, FUNCTION, CATALYTIC ACTIVITY,
RP COFACTOR, AND MUTAGENESIS OF ARG-307; HIS-308 AND SER-309.
RX PubMed=21810411; DOI=10.1016/j.bbrc.2011.07.071;
RA Bhatt V.S., Guan W., Xue M., Yuan H., Wang P.G.;
RT "Insights into role of the hydrogen bond networks in substrate recognition
RT by UDP-GalNAc 4-epimerases.";
RL Biochem. Biophys. Res. Commun. 412:232-237(2011).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) IN COMPLEX WITH NAD AND
RP UDP-N-ACETYL-ALPHA-D-GALACTOSAMINE, COFACTOR, SUBUNIT, AND PATHWAY.
RX PubMed=21384454; DOI=10.1002/pro.611;
RA Bhatt V.S., Guo C.Y., Guan W., Zhao G., Yi W., Liu Z.J., Wang P.G.;
RT "Altered architecture of substrate binding region defines the unique
RT specificity of UDP-GalNAc 4-epimerases.";
RL Protein Sci. 20:856-866(2011).
CC -!- FUNCTION: Catalyzes the epimerization of UDP-N-acetylglucosamine (UDP-
CC GlcNAc) to UDP-N-acetylgalactosamine (UDP-GalNAc). Has very low
CC epimerase activity with UDP-Glc and UDP-Gal. Plays a role in the
CC biosynthesis of 2-acetamino-2-deoxy-L-altruronic acid, a building block
CC of the O-antigen in bacterial lipopolysaccharide (LPS).
CC {ECO:0000269|PubMed:12484781, ECO:0000269|PubMed:21810411,
CC ECO:0000305}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=UDP-N-acetyl-alpha-D-glucosamine = UDP-N-acetyl-alpha-D-
CC galactosamine; Xref=Rhea:RHEA:20517, ChEBI:CHEBI:57705,
CC ChEBI:CHEBI:67138; EC=5.1.3.7; Evidence={ECO:0000269|PubMed:12484781,
CC ECO:0000269|PubMed:21810411};
CC -!- COFACTOR:
CC Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC Evidence={ECO:0000269|PubMed:12484781, ECO:0000269|PubMed:21384454,
CC ECO:0000269|PubMed:21810411};
CC Note=Binds 1 NAD(+) per subunit. {ECO:0000269|PubMed:12484781,
CC ECO:0000269|PubMed:21384454, ECO:0000269|PubMed:21810411};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=131 uM for UDP-GalNAc {ECO:0000269|PubMed:12484781};
CC KM=137 uM for UDP-GalNAc {ECO:0000269|PubMed:12484781};
CC Note=kcat is 461 sec(-1) with UDP-GlcNAc. kcat is 1038 sec(-1) with
CC UDP-GalNAc. {ECO:0000269|PubMed:12484781};
CC pH dependence:
CC Optimum pH is 7.0-9.0. {ECO:0000269|PubMed:12484781};
CC Temperature dependence:
CC Optimum temperature is 37 degrees Celsius.
CC {ECO:0000269|PubMed:12484781};
CC -!- PATHWAY: Bacterial outer membrane biogenesis; LPS O-antigen
CC biosynthesis. {ECO:0000303|PubMed:12484781,
CC ECO:0000303|PubMed:21384454, ECO:0000305}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:12484781,
CC ECO:0000269|PubMed:21384454}.
CC -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase
CC family. {ECO:0000305}.
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DR EMBL; AF285970; AAG17409.1; -; Genomic_DNA.
DR PDB; 3LU1; X-ray; 2.50 A; A/B/C/D=1-345.
DR PDB; 3RU7; X-ray; 2.60 A; A/B/C/D=1-345.
DR PDB; 3RU9; X-ray; 2.21 A; A/B/C/D=1-345.
DR PDB; 3RUA; X-ray; 2.10 A; A/B/C/D=1-345.
DR PDB; 3RUC; X-ray; 2.10 A; A/B/C/D=1-345.
DR PDB; 3RUD; X-ray; 2.30 A; A/B/C/D=1-345.
DR PDB; 3RUE; X-ray; 2.80 A; A/B/S/b=1-345.
DR PDB; 3RUF; X-ray; 2.00 A; A/B/S/b=1-345.
DR PDB; 3RUH; X-ray; 2.88 A; A/B/C/D=1-345.
DR PDBsum; 3LU1; -.
DR PDBsum; 3RU7; -.
DR PDBsum; 3RU9; -.
DR PDBsum; 3RUA; -.
DR PDBsum; 3RUC; -.
DR PDBsum; 3RUD; -.
DR PDBsum; 3RUE; -.
DR PDBsum; 3RUF; -.
DR PDBsum; 3RUH; -.
DR AlphaFoldDB; Q7BJX9; -.
DR SMR; Q7BJX9; -.
DR BioCyc; MetaCyc:MON-13183; -.
DR BRENDA; 5.1.3.7; 4904.
DR UniPathway; UPA00281; -.
DR EvolutionaryTrace; Q7BJX9; -.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0003974; F:UDP-N-acetylglucosamine 4-epimerase activity; IEA:UniProtKB-EC.
DR GO; GO:0009243; P:O antigen biosynthetic process; IEA:UniProtKB-UniPathway.
DR InterPro; IPR001509; Epimerase_deHydtase.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR Pfam; PF01370; Epimerase; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Isomerase; NAD; Nucleotide-binding.
FT CHAIN 1..345
FT /note="UDP-N-acetylglucosamine 4-epimerase"
FT /id="PRO_0000430851"
FT BINDING 26..31
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:21384454,
FT ECO:0000269|PubMed:21810411, ECO:0000312|PDB:3LU1,
FT ECO:0000312|PDB:3RU7, ECO:0000312|PDB:3RU9,
FT ECO:0000312|PDB:3RUA, ECO:0000312|PDB:3RUC,
FT ECO:0000312|PDB:3RUD, ECO:0000312|PDB:3RUE,
FT ECO:0000312|PDB:3RUF, ECO:0000312|PDB:3RUH"
FT BINDING 50..55
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:21384454,
FT ECO:0000269|PubMed:21810411, ECO:0000312|PDB:3LU1,
FT ECO:0000312|PDB:3RU7, ECO:0000312|PDB:3RU9,
FT ECO:0000312|PDB:3RUA, ECO:0000312|PDB:3RUC,
FT ECO:0000312|PDB:3RUD, ECO:0000312|PDB:3RUE,
FT ECO:0000312|PDB:3RUF, ECO:0000312|PDB:3RUH"
FT BINDING 81..82
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:21384454,
FT ECO:0000269|PubMed:21810411, ECO:0000312|PDB:3LU1,
FT ECO:0000312|PDB:3RU7, ECO:0000312|PDB:3RU9,
FT ECO:0000312|PDB:3RUA, ECO:0000312|PDB:3RUC,
FT ECO:0000312|PDB:3RUD, ECO:0000312|PDB:3RUE,
FT ECO:0000312|PDB:3RUF, ECO:0000312|PDB:3RUH"
FT BINDING 101..103
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:21384454,
FT ECO:0000269|PubMed:21810411, ECO:0000312|PDB:3LU1,
FT ECO:0000312|PDB:3RU7, ECO:0000312|PDB:3RU9,
FT ECO:0000312|PDB:3RUA, ECO:0000312|PDB:3RUC,
FT ECO:0000312|PDB:3RUD, ECO:0000312|PDB:3RUE,
FT ECO:0000312|PDB:3RUF, ECO:0000312|PDB:3RUH"
FT BINDING 120
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:21384454,
FT ECO:0000269|PubMed:21810411, ECO:0000312|PDB:3RUA,
FT ECO:0000312|PDB:3RUC"
FT BINDING 145..146
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:21384454,
FT ECO:0000269|PubMed:21810411"
FT BINDING 169
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:21384454,
FT ECO:0000269|PubMed:21810411, ECO:0000312|PDB:3LU1,
FT ECO:0000312|PDB:3RU7, ECO:0000312|PDB:3RU9,
FT ECO:0000312|PDB:3RUA, ECO:0000312|PDB:3RUC,
FT ECO:0000312|PDB:3RUD, ECO:0000312|PDB:3RUE,
FT ECO:0000312|PDB:3RUF, ECO:0000312|PDB:3RUH"
FT BINDING 173
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:21384454,
FT ECO:0000269|PubMed:21810411, ECO:0000312|PDB:3LU1,
FT ECO:0000312|PDB:3RU7, ECO:0000312|PDB:3RU9,
FT ECO:0000312|PDB:3RUA, ECO:0000312|PDB:3RUC,
FT ECO:0000312|PDB:3RUD, ECO:0000312|PDB:3RUE,
FT ECO:0000312|PDB:3RUF, ECO:0000312|PDB:3RUH"
FT BINDING 196..198
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:21384454,
FT ECO:0000269|PubMed:21810411"
FT BINDING 199
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:21384454,
FT ECO:0000269|PubMed:21810411, ECO:0000312|PDB:3LU1,
FT ECO:0000312|PDB:3RU7, ECO:0000312|PDB:3RU9,
FT ECO:0000312|PDB:3RUA, ECO:0000312|PDB:3RUC,
FT ECO:0000312|PDB:3RUD, ECO:0000312|PDB:3RUE,
FT ECO:0000312|PDB:3RUF, ECO:0000312|PDB:3RUH"
FT BINDING 213..216
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:21384454,
FT ECO:0000269|PubMed:21810411"
FT BINDING 228..230
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:21384454,
FT ECO:0000269|PubMed:21810411"
FT BINDING 237
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:21384454,
FT ECO:0000269|PubMed:21810411"
FT BINDING 302..305
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:21384454,
FT ECO:0000269|PubMed:21810411"
FT MUTAGEN 147
FT /note="S->T: No effect on epimerase activity."
FT /evidence="ECO:0000269|PubMed:21810411"
FT MUTAGEN 236
FT /note="S->G: No effect on epimerase activity."
FT /evidence="ECO:0000269|PubMed:21810411"
FT MUTAGEN 271
FT /note="R->G: No effect on epimerase activity."
FT /evidence="ECO:0000269|PubMed:21810411"
FT MUTAGEN 307
FT /note="R->A: No effect on epimerase activity."
FT /evidence="ECO:0000269|PubMed:21810411"
FT MUTAGEN 308
FT /note="H->A: No effect on epimerase activity."
FT /evidence="ECO:0000269|PubMed:21810411"
FT MUTAGEN 309
FT /note="S->Y: Abolishes epimerase activity."
FT /evidence="ECO:0000269|PubMed:21810411"
FT HELIX 6..17
FT /evidence="ECO:0007829|PDB:3RUF"
FT STRAND 21..25
FT /evidence="ECO:0007829|PDB:3RUF"
FT TURN 26..28
FT /evidence="ECO:0007829|PDB:3RUF"
FT HELIX 30..41
FT /evidence="ECO:0007829|PDB:3RUF"
FT STRAND 45..50
FT /evidence="ECO:0007829|PDB:3RUF"
FT STRAND 52..54
FT /evidence="ECO:0007829|PDB:3RUC"
FT HELIX 57..65
FT /evidence="ECO:0007829|PDB:3RUF"
FT HELIX 69..72
FT /evidence="ECO:0007829|PDB:3RUF"
FT STRAND 75..79
FT /evidence="ECO:0007829|PDB:3RUF"
FT HELIX 85..91
FT /evidence="ECO:0007829|PDB:3RUF"
FT TURN 92..94
FT /evidence="ECO:0007829|PDB:3RUF"
FT STRAND 96..100
FT /evidence="ECO:0007829|PDB:3RUF"
FT HELIX 107..112
FT /evidence="ECO:0007829|PDB:3RUF"
FT HELIX 114..121
FT /evidence="ECO:0007829|PDB:3RUF"
FT HELIX 123..134
FT /evidence="ECO:0007829|PDB:3RUF"
FT STRAND 138..145
FT /evidence="ECO:0007829|PDB:3RUF"
FT HELIX 146..149
FT /evidence="ECO:0007829|PDB:3RUF"
FT STRAND 155..157
FT /evidence="ECO:0007829|PDB:3RUF"
FT HELIX 168..187
FT /evidence="ECO:0007829|PDB:3RUF"
FT STRAND 192..196
FT /evidence="ECO:0007829|PDB:3RUF"
FT STRAND 198..201
FT /evidence="ECO:0007829|PDB:3RUF"
FT HELIX 213..223
FT /evidence="ECO:0007829|PDB:3RUF"
FT STRAND 228..233
FT /evidence="ECO:0007829|PDB:3RUF"
FT HELIX 242..253
FT /evidence="ECO:0007829|PDB:3RUF"
FT HELIX 257..259
FT /evidence="ECO:0007829|PDB:3RUF"
FT STRAND 261..267
FT /evidence="ECO:0007829|PDB:3RUF"
FT HELIX 274..286
FT /evidence="ECO:0007829|PDB:3RUF"
FT STRAND 297..299
FT /evidence="ECO:0007829|PDB:3RUF"
FT HELIX 314..320
FT /evidence="ECO:0007829|PDB:3RUF"
FT HELIX 328..343
FT /evidence="ECO:0007829|PDB:3RUF"
SQ SEQUENCE 345 AA; 38949 MW; 90A364D247CCA810 CRC64;
MDIYMSRYEE ITQQLIFSPK TWLITGVAGF IGSNLLEKLL KLNQVVIGLD NFSTGHQYNL
DEVKTLVSTE QWSRFCFIEG DIRDLTTCEQ VMKGVDHVLH QAALGSVPRS IVDPITTNAT
NITGFLNILH AAKNAQVQSF TYAASSSTYG DHPALPKVEE NIGNPLSPYA VTKYVNEIYA
QVYARTYGFK TIGLRYFNVF GRRQDPNGAY AAVIPKWTAA MLKGDDVYIN GDGETSRDFC
YIDNVIQMNI LSALAKDSAK DNIYNVAVGD RTTLNELSGY IYDELNLIHH IDKLSIKYRE
FRSGDVRHSQ ADVTKAIDLL KYRPNIKIRE GLRLSMPWYV RFLKG
